Scalar Relativistic All-Electron and Pseudopotential Ab Initio Study of a Minimal Nitrogenase [Fe(SH)₄H]^- Model Employing Coupled-Cluster and Auxiliary-Field Quantum Monte Carlo Many-Body Methods.

ABSTRACT: Nitrogenase is the only enzyme that can cleave the triple bond in N₂, making nitrogen available to organisms. The detailed mechanism of this enzyme is currently not known, and computational studies are complicated by the fact that different density functional theory (DFT) methods give very different energetic results for calculations involving nitrogenase models. Recently, we designed a [Fe(SH)₄H]^- model with the fifth proton binding either to Fe or S to mimic different possible protonation states of the nitrogenase active site. We showed that the energy difference between these two isomers (ΔE) is hard to estimate with quantum-mechanical methods. Based on nonrelativistic single-reference coupled-cluster (CC) calculations, we estimated that the ΔE

SUBMITTER: Vysotskiy VP 

PROVIDER: S-EPMC10895656 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature